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Research Article

Design, synthesis, spectroscopic characterizations, in vitro pancreatic lipase as well as tyrosinase inhibition evaluations and in silico analysis of novel aryl sulfonate-naphthalene hybrids

ORCID Icon, , & ORCID Icon
Pages 7128-7143 | Received 24 May 2022, Accepted 18 Aug 2022, Published online: 07 Sep 2022
 

Abstract

One of the primary purposes of this study is to synthesize new aryl sulfonate-naphthalene hybrid structures possessing divergent electron-withdrawing and electron-releasing functional groups. Following the improved reaction conditions, we successfully gathered ten distinct sulfonate derivatives (3a-j) with good yields. The synthesized naphthalene-based sulfonate derivatives were then characterized using appropriate analytical methods (FT-IR, 1H-NMR, 13C-NMR, HRMS, and elemental analysis). Additionally, in vitro and in silico enzyme inhibitory properties of the prepared aryl sulfonate-naphthalene hybrid structures were evaluated against pancreatic lipase and tyrosinase enzymes. Corresponding in vitro enzyme activity investigations revealed that the produced compounds inhibit pancreatic lipase and tyrosinase enzymes significantly. According to the lowest IC50 values, 3h (95.3 ± 4.0 µM) demonstrated the most effective inhibition against pancreatic lipase, whereas 3a (40.8 ± 3.3 µM) was found as the most effective inhibition against the tyrosinase. According to in silico studies, 3a exhibited the highest affinity value (−9.9 kcal/mol) against pancreatic lipase, whereas 3f demonstrated the best affinity value (−8.7 kcal/mol) against tyrosinase.

Furthermore, we investigated various structural and physicochemical properties of the target molecules, namely frontier orbital’ (HOMO, LUMO, and bandgap) energies (including their corresponding contour plots), global reactivity descriptors (ionization energy and electron affinity), and electronegativity values gathered from ground-state (GS) density functional theory (DFT) calculations. These investigations demonstrated that the observed electrostatic interactions effectively contributed to the studied molecules’ experimentally demonstrated enzyme inhibition potential. Also, ADMET studies were evaluated to enlighten the molecular interactions of the compounds with the enzymes.

Communicated by Ramaswamy H. Sarma

Acknowledgment

The authors would like to thank the Eastern Anatolia High Technology Application and Research Center (DAYTAM) for HRMS and CHNS elemental analyses. The authors would like to thank the Mus Alparslan University Central Laboratory for the spectrometry analyses. The quantum chemical calculations reported in this paper were executed at TUBITAK ULAKBIM, High Performance and Grid Computing Center (TRUBA resources).

Disclosure statement

No potential conflict of interest was reported by the authors.

Funding

The author(s) reported there is no funding associated with the work featured in this article.

Authors contribution

Adem Korkmaz carried out the design, synthesis, analysis, enzyme inhibitions experiments, review, process, ADMET, molecular docking studies, writing and editing processes of the manuscript.

Gülbin Kurtay executed quantum chemical (DFT) calculations. She also contributed to the writing and editing processes of the manuscript.

Esin Kaya contributed to the chemical synthesis and editing of the article.

Ercan Bursal carried out the in vitro enzyme inhibition and in silico molecular docking studies and editing the paper.

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